C11orf16
| C11orf16 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | C11orf16, chromosome 11 open reading frame 16 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | MGI: 1928824; HomoloGene: 49631; GeneCards: C11orf16; OMA:C11orf16 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Gene C11orf16, chromosome 11 open reading frame 16, is a protein in humans that is encoded by the C11orf16 gene.[5][6] It has 7 exons, and the size of 467 amino acids.
Gene
[edit]Location
[edit]The gene C11orf16 is located on chromosome 11(p15.4), starting at 8,920,076bp and ending at 8,933,006bp.
Gene neighborhood
[edit]Gene ASCL3 and AKIP1 are the neighbor genes of C11orf16 on chromosome 11.
Expression
[edit]Human
[edit]The gene does not have high expression throughout the body tissues. The percentile rank within the sample are higher in pancreas, ovary, and appendix.
Mouse brain
[edit]Even though the gene does not have a significant high expression in the mouse brain, it is most expressed in midbrain, isocortex, olfactory areas, and medulla.
Transcription factors
[edit]Some transcription factors that have the higher matrix similarity are Kruppel-like zinc finger protein 219, zinc finger protein 263, ZKSCAN12 (zinc finger protein with KRAB and SCAN domains 12), chorion-specific transcription factor GCMa, and Ras-responsive element binding protein 1.[7]
mRNA
[edit]The predicted C11orf16 transcript variant X1 is 2386bp long and has NCBI accession number of XM_017018013.1.[8]
Homology
[edit]Paralogs
[edit]No paralogs were found for the C11orf16 gene through NCBI BLAST.
| Description | Common name | NCBI accession ID | Query cover | E value | Identity | Date of divergence (MYA) |
|---|---|---|---|---|---|---|
| Homo sapiens | Human | NP_065694.2 | 100 % | 0 | 100% | N/A |
| Pongo abelii | Sumatran orangutan | PNJ24628 | 84% | 0 | 95% | 15.2 |
| Aotus nancymaae | Nancy Ma's night monkey | XP_012312127.1 | 88% | 0 | 84% | 42.6 |
| Chinchilla lanigera | Long-tailed chinchilla | XP_013367496.1 | 97% | 0 | 68% | 88 |
| Equus przewalskii | Przewalski's horse | XP_008512245.1 | 98% | 0 | 73% | 94 |
| Cervus elaphus hippelaphus | Central European red deer | OWK17675.1 | 99% | 0 | 67% | 94 |
| Hipposideros armiger | Great roundleaf bat | XP_019511755.1 | 99% | 0 | 65% | 94 |
| Neomonachus schauinslandi | Hawaiian monk seal | XP_021541375.1 | 99% | 0 | 66% | 94 |
| Lipotes vexillifer | Baiji | XP_007459933.1 | 98% | 0 | 68% | 94 |
| Myotis brandtii | Brandt's bat | XP_005874017.1 | 98% | 1e-174 | 67% | 94 |
| Chelonia mydas | Green sea turtle | XP_007057171.1 | 83% | 1e-57 | 37% | 320 |
| Balearica regulorum gibbericeps | Grey crowned crane | XP_010311948.1 | 70% | 6e-5 | 40% | 320 |
Conservation
[edit]The gene C11orf16 is conserved in many animal species including mammals, avians, and reptiles.
Protein
[edit]Molecular weight
[edit]The predicted molecular weight of the protein encoded by C11orf16 is 51 kilodaltons.[9][10]
Domains and motifs
[edit]Several protein domains and motifs were found including CHD5-like protein, tyrosine kinase phosphorylation site, protein kinase C phosphorylation site, N-myristoylation site, casein kinase II phosphorylation site, and cGMP-dependent protein kinase phosphorylation site.[11] The picture indicates the location of the motifs.
Secondary structure
[edit]The protein is predicted to be made up with 21.2% of alpha helix, 15.2% of extended strand, and 63% of random coil.
Post-translational modifications
[edit]No transmembrane helices,[12] potential GPI-modification sites, or TM-proteins were found. There were seven predicted sumoylation sites,[13] multiple phosporylation sites with most of them being unspecified,[citation needed] and nine glycosylation sites.[14]
Subcellular localization predictor
[edit]The protein is predicted to be localized to the nucleus with the probability of 47.8%; mitochondria with the probability of 26.1%.[16]
Protein interaction
[edit]Proteins C1orf105 (Chromosome 1 open reading frame 105), PWWP2A, and SMYD1(SET and MYND domain containing 1) were found to be interacting with C11orf16.[17]
Clinical significance
[edit]Disease association
[edit]Protein coded by C11orf16 gene is also predicted to have 19.61% sequence identity to tumor suppressor p53-binding protein suggesting that this gene might be involved with tumor suppressing process.[18]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000176029 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031022 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Amid C, Bahr A, Mujica A, Sampson N, Bikar SE, Winterpacht A, Zabel B, Hankeln T, Schmidt ER (Aug 2001). "Comparative genomic sequencing reveals a strikingly similar architecture of a conserved syntenic region on human chromosome 11p15.3 (including gene ST5) and mouse chromosome 7". Cytogenet Cell Genet. 93 (3–4): 284–90. doi:10.1159/000056999. PMID 11528127. S2CID 27611036.
- ^ "Entrez Gene: C11orf16 chromosome 11 open reading frame 16".
- ^ "Genomatix". Archived from the original on 2021-08-17. Retrieved 2018-05-06.
- ^ "NCBI Nucleotide". 22 November 2021.
- ^ "Expasy".
- ^ "Sigma Antibodies".
- ^ "Motif Scan".
- ^ "TMHMM".
- ^ "SUMOplot".
- ^ "YingOYang".
- ^ "Protter".
- ^ "PSORTII".[permanent dead link]
- ^ "String".
- ^ "SWISS-MODEL". Archived from the original on 2018-05-07. Retrieved 2018-05-06.
External links
[edit]- Human C11orf16 genome location and C11orf16 gene details page in the UCSC Genome Browser.
- C11orf16 information on GeneCards
Further reading
[edit]- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.